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Article ; Online: Improved clinical trial race/ethnicity reporting and updated inclusion profile, 2017-2022: A New Jersey snapshot.

Paleoudis, Elli Gourna / Han, Zhiyong / Gelman, Simon / Arias-Ruiz, Hernan / Carter, Destiney / Bertrand, Jovan / Mastrogiovanni, Nicole / Terlecky, Stanley R

Global epidemiology

2023 Volume 7, Page(s) 100134

Abstract: Background: Diverse representation in clinical trials is an important goal in the testing of a medical, diagnostic, or therapeutic intervention. To date, the desired level of trial equity and inclusivity has been unevenly achieved.: Methods: ... ...

Abstract	Background: Diverse representation in clinical trials is an important goal in the testing of a medical, diagnostic, or therapeutic intervention. To date, the desired level of trial equity and inclusivity has been unevenly achieved. Methods: Employing the US National Library of Medicine's Clinicaltrials.gov registry, we examined 481 clinical trials conducted - at least in part - in the state of New Jersey. These trials were initiated after the FDA-mandated Common Rule changes, i.e., between January 2017 and October 2022, were enacted, and had their results posted. We analyzed sex/race/ethnicity reporting as well as applicable enrollment. Using meta-analysis, we estimated group participation proportions of a subset of the 481 identified trials; specifically, the 229 studies that were conducted solely within the US (i.e., without international sites) and compared them to US census data. Findings: Within the 481 clinical trials analyzed, over 97% reported on the race and/or ethnicity of their enrollees; all included information on sex. Reporting was not affected by funding source or therapeutic area. Based on the 229 solely US-based studies, the participants overall were 76.7% White; 14.1% Black; 2.7% Asian; and 15% Hispanic. Inclusion of Black participants did not differ from the 2020 US census data; in contrast, the levels of Asian and Hispanic participation were below the corresponding census percentages. Interpretation: The past five years have seen an overall uptick in the equity of race/ethnicity reporting and inclusivity of clinical trials, as compared to previously reported data, presaging the potential acquisition of ever more powerful and meaningful results of such interventional studies going forward. Funding: Support for this study comes from the Hackensack Meridian Research in context: Evidence before this study
Language	English
Publishing date	2023-12-23
Publishing country	United States
Document type	Journal Article
ISSN	2590-1133
ISSN (online)	2590-1133
DOI	10.1016/j.gloepi.2023.100134
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Article ; Online: Clinical Outcomes of COVID-19 Patients with Pre-existing, Compromised Immune Systems: A Review of Case Reports.

Corse, Tanner / Dayan, Linda / Kersten, Sydney / Battaglia, Fortunato / Terlecky, Stanley R / Han, Zhiyong

International journal of medical sciences

2020 Volume 17, Issue 18, Page(s) 2974–2986

Abstract: In the ongoing COVID-19 pandemic, all COVID-19 patients are naïve patients as it is the first-time humans have been exposed to the SARS-CoV-2 virus. As with exposure to many viruses, individuals with pre-existing, compromised immune systems may be at ... ...

Abstract	In the ongoing COVID-19 pandemic, all COVID-19 patients are naïve patients as it is the first-time humans have been exposed to the SARS-CoV-2 virus. As with exposure to many viruses, individuals with pre-existing, compromised immune systems may be at increased risk of developing severe symptoms and/or dying because of (SARS-CoV-2) infection. To learn more about such individuals, we conducted a search and review of published reports on the clinical characteristics and outcomes of COVID-19 patients with pre-existing, compromised immune systems. Here we present our review of patients who possess pre-existing primary antibody deficiency (PAD) and those who are organ transplant recipients on maintenance immunosuppressants. Our review indicates different clinical outcomes for the patients with pre-existing PAD, depending on the underlying causes. For organ transplant recipients, drug-induced immune suppression alone does not appear to enhance COVID-19 mortality risk - rather, advanced age, comorbidities, and the development of secondary complications appears required.
MeSH term(s)	Betacoronavirus/immunology ; Betacoronavirus/physiology ; COVID-19 ; Comorbidity ; Coronavirus Infections/complications ; Coronavirus Infections/diagnosis ; Coronavirus Infections/epidemiology ; Coronavirus Infections/immunology ; Humans ; Immune System Diseases/complications ; Immune System Diseases/diagnosis ; Immunocompromised Host/immunology ; Immunosuppressive Agents/therapeutic use ; Mortality ; Pandemics ; Pneumonia, Viral/complications ; Pneumonia, Viral/diagnosis ; Pneumonia, Viral/epidemiology ; Pneumonia, Viral/immunology ; Primary Immunodeficiency Diseases/complications ; Primary Immunodeficiency Diseases/diagnosis ; Primary Immunodeficiency Diseases/immunology ; Primary Immunodeficiency Diseases/mortality ; Prognosis ; SARS-CoV-2 ; Transplant Recipients/statistics & numerical data
Chemical Substances	Immunosuppressive Agents
Keywords	covid19
Language	English
Publishing date	2020-10-18
Publishing country	Australia
Document type	Journal Article ; Review
ZDB-ID	2151424-0
ISSN	1449-1907 ; 1449-1907
ISSN (online)	1449-1907
ISSN	1449-1907
DOI	10.7150/ijms.50537
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Article: Clinical Outcomes of COVID-19 Patients with Pre-existing, Compromised Immune Systems: A Review of Case Reports

Corse, Tanner / Dayan, Linda / Kersten, Sydney / Battaglia, Fortunato / Terlecky, Stanley R / Han, Zhiyong

Int J Med Sci

Abstract	In the ongoing COVID-19 pandemic, all COVID-19 patients are naïve patients as it is the first-time humans have been exposed to the SARS-CoV-2 virus. As with exposure to many viruses, individuals with pre-existing, compromised immune systems may be at increased risk of developing severe symptoms and/or dying because of (SARS-CoV-2) infection. To learn more about such individuals, we conducted a search and review of published reports on the clinical characteristics and outcomes of COVID-19 patients with pre-existing, compromised immune systems. Here we present our review of patients who possess pre-existing primary antibody deficiency (PAD) and those who are organ transplant recipients on maintenance immunosuppressants. Our review indicates different clinical outcomes for the patients with pre-existing PAD, depending on the underlying causes. For organ transplant recipients, drug-induced immune suppression alone does not appear to enhance COVID-19 mortality risk - rather, advanced age, comorbidities, and the development of secondary complications appears required.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #902898
Database	COVID19

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Article ; Online: Targeted intracellular catalase delivery protects neonatal rat myocytes from hypoxia-reoxygenation and ischemia-reperfusion injury.

Undyala, Vishnu / Terlecky, Stanley R / Vander Heide, Richard S

Cardiovascular pathology : the official journal of the Society for Cardiovascular Pathology

2010 Volume 20, Issue 5, Page(s) 272–280

Abstract: Unlabelled: Hypoxia followed by reoxygenation and ischemia reperfusion cause cell death in neonatal rat ventricular myocytes primarily through the generation of oxidative stress. Extracellular catalase has not been effective in reducing or eliminating ... ...

Abstract	Unlabelled: Hypoxia followed by reoxygenation and ischemia reperfusion cause cell death in neonatal rat ventricular myocytes primarily through the generation of oxidative stress. Extracellular catalase has not been effective in reducing or eliminating ischemia reperfusion- or hypoxia-reoxygenation-induced cell death due both to extracellular degradation and to poor cellular uptake. Aims: (1) To determine whether a cell-penetrating catalase derivative with enhanced peroxisome targeting efficiency (catalase-SKL) increases intracellular levels of the antioxidant enzyme in neonatal rat ventricular myocytes; and (2) to determine whether catalase-SKL protects against both hypoxia-reoxygenation and ischemia reperfusion injury. Methods: Neonatal rat ventricular myocytes were subjected to 3 or 6 h of hypoxia-reoxygenation or to 1 h of ischemia reperfusion. Extracellular catalase concentration, activity, and subcellular distribution were determined using standard techniques. Reactive oxygen species and related oxidative stress were visualized using 2',7'-dichlorofluorescin diacetate. Cell death was measured using trypan blue exclusion or lactate dehydrogenase release assays. Results: Extracellular catalase activity was higher in (catalase-SKL) transduced myocytes, was concentrated in a membranous cellular fraction, and potently inhibited oxidative stress. In contrast to nontransducible (unmodified) extracellular catalase, catalase-SKL-treated myocytes were protected against both hypoxia-reoxygenation and ischemia reperfusion. Conclusions: (1) Catalase-SKL increased myocyte extracellular catalase content and activity and dramatically increased resistance to hydrogen peroxide-induced oxidation; (2) catalase-SKL protects against both hypoxia-reoxygenation and ischemia reperfusion; (3) catalase-SKL may represent a new therapeutic approach to protect hearts against myocardial hypoxia-reoxygenation or ischemia reperfusion.
MeSH term(s)	Animals ; Animals, Newborn ; Catalase/administration & dosage ; Catalase/pharmacology ; Cell Hypoxia/drug effects ; Cell Hypoxia/physiology ; Cell Survival/drug effects ; Cells, Cultured ; Drug Carriers ; Heart Ventricles/cytology ; Hydrogen Peroxide/pharmacology ; Molecular Targeted Therapy ; Myocardial Reperfusion Injury/drug therapy ; Myocardial Reperfusion Injury/metabolism ; Myocytes, Cardiac/drug effects ; Myocytes, Cardiac/enzymology ; Myocytes, Cardiac/pathology ; Oxidative Stress/drug effects ; Rats ; Targeted Gene Repair ; Transduction, Genetic
Chemical Substances	Drug Carriers ; Hydrogen Peroxide (BBX060AN9V) ; Catalase (EC 1.11.1.6)
Language	English
Publishing date	2010-08-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	1134600-0
ISSN	1879-1336 ; 1054-8807
ISSN (online)	1879-1336
ISSN	1054-8807
DOI	10.1016/j.carpath.2010.06.011
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Article: Hsp70s and lysosomal proteolysis.

Terlecky, S R

Experientia

1994 Volume 50, Issue 11-12, Page(s) 1021–1025

Abstract: Confluent cultured cells activate a lysosomal pathway of polypeptide breakdown in response to withdrawal of serum growth factors. The substrates for this proteolytic pathway are a restricted class of cytosolic polypeptides containing peptide sequences ... ...

Abstract	Confluent cultured cells activate a lysosomal pathway of polypeptide breakdown in response to withdrawal of serum growth factors. The substrates for this proteolytic pathway are a restricted class of cytosolic polypeptides containing peptide sequences biochemically related to lysine-phenylalanine-glutamate-arginine-glutamine, or, in single amino acid abbreviations, KFERQ. The heat shock cognate protein of 73 kD (hsc73) binds to a variety of polypeptides via this molecular determinant and facilitates their lysosomal import and degradation. In addition, a portion of intracellular hsc73 resides within the lysosome and appears to be an essential component of the proteolytic machinery. Several potential mechanisms by which hsc73 mediates selective lysosomal import and degradation of polypeptides are discussed.
MeSH term(s)	Amino Acid Sequence ; Animals ; Biological Transport ; HSP70 Heat-Shock Proteins/physiology ; Humans ; Lysosomes/metabolism ; Molecular Sequence Data ; Oligopeptides/metabolism ; Proteins/metabolism
Chemical Substances	HSP70 Heat-Shock Proteins ; Oligopeptides ; Proteins
Language	English
Publishing date	1994-11-30
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1972-0
ISSN	0014-4754
ISSN	0014-4754
DOI	10.1007/bf01923456
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Article ; Online: Progeric effects of catalase inactivation in human cells.

Koepke, Jay I / Wood, Christopher S / Terlecky, Laura J / Walton, Paul A / Terlecky, Stanley R

Toxicology and applied pharmacology

2008 Volume 232, Issue 1, Page(s) 99–108

Abstract: Peroxisomes generate hydrogen peroxide, a reactive oxygen species, as part of their normal metabolism. A number of pathological situations exist in which the organelle's capacity to degrade the potentially toxic oxidant is compromised. It is the ... ...

Abstract	Peroxisomes generate hydrogen peroxide, a reactive oxygen species, as part of their normal metabolism. A number of pathological situations exist in which the organelle's capacity to degrade the potentially toxic oxidant is compromised. It is the peroxidase, catalase, which largely determines the functional antioxidant capacity of the organelle, and it is this enzyme that is affected in aging, in certain diseases, and in response to exposure to specific chemical agents. To more tightly control the enzymatic activity of peroxisomal catalase and carefully document the effects of its impaired action on human cells, we employed the inhibitor 3-amino-1,2,4-triazole. We show that by chronically reducing catalase activity to approximately 38% of normal, cells respond in a dramatic manner, displaying a cascade of accelerated aging reactions. Hydrogen peroxide and related reactive oxygen species are produced, protein and DNA are oxidatively damaged, import into peroxisomes and organelle biogenesis is corrupted, and matrix metalloproteinases are hyper-secreted from cells. In addition, mitochondria are functionally impaired, losing their ability to maintain a membrane potential and synthesize reactive oxygen species themselves. These latter results suggest an important redox-regulated connection between the two organelle systems, a topic of considerable interest for future study.
MeSH term(s)	Amitrole/pharmacology ; Catalase/antagonists & inhibitors ; Catalase/metabolism ; Cell Line ; Cell Proliferation/drug effects ; Cellular Senescence/drug effects ; DNA Damage ; Dose-Response Relationship, Drug ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Fibroblasts/drug effects ; Fibroblasts/enzymology ; Humans ; Hydrogen Peroxide/metabolism ; Matrix Metalloproteinase 2/metabolism ; Membrane Potential, Mitochondrial/drug effects ; Mitochondria/drug effects ; Mitochondria/metabolism ; Oxidation-Reduction ; Oxidative Stress/drug effects ; Peroxisome-Targeting Signal 1 Receptor ; Peroxisomes/drug effects ; Peroxisomes/enzymology ; Reactive Oxygen Species/metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Time Factors
Chemical Substances	Enzyme Inhibitors ; Peroxisome-Targeting Signal 1 Receptor ; Reactive Oxygen Species ; Receptors, Cytoplasmic and Nuclear ; Hydrogen Peroxide (BBX060AN9V) ; Catalase (EC 1.11.1.6) ; MMP2 protein, human (EC 3.4.24.24) ; Matrix Metalloproteinase 2 (EC 3.4.24.24) ; Amitrole (ZF80H5GXUF)
Language	English
Publishing date	2008-10-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	204477-8
ISSN	1096-0333 ; 0041-008X
ISSN (online)	1096-0333
ISSN	0041-008X
DOI	10.1016/j.taap.2008.06.004
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Article: How peroxisomes arise.

Terlecky, S R / Fransen, M

Traffic (Copenhagen, Denmark)

2001 Volume 1, Issue 6, Page(s) 465–473

Abstract: Peroxisomes are formed by the synthesis and assembly of membrane proteins and lipids, the selective import of proteins from the cytosol, and the growth and division of resultant organelles. To date, 23 proteins, called peroxins, are known to participate ... ...

Abstract	Peroxisomes are formed by the synthesis and assembly of membrane proteins and lipids, the selective import of proteins from the cytosol, and the growth and division of resultant organelles. To date, 23 proteins, called peroxins, are known to participate in these processes. This review summarizes recent progress in peroxin characterization and examines the underlying molecular mechanisms of peroxisome biosynthesis.
MeSH term(s)	Animals ; Biological Transport, Active ; Humans ; In Vitro Techniques ; Membrane Lipids/metabolism ; Membrane Proteins/metabolism ; Models, Biological ; Peroxisomes/metabolism ; Receptors, Cell Surface/metabolism ; Signal Transduction
Chemical Substances	Membrane Lipids ; Membrane Proteins ; Receptors, Cell Surface ; peroxisomal targeting sequence receptor
Language	English
Publishing date	2001-01-31
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1034/j.1600-0854.2000.010604.x
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Article: PTS2 protein import into mammalian peroxisomes.

Legakis, J E / Terlecky, S R

Traffic (Copenhagen, Denmark)

2001 Volume 2, Issue 4, Page(s) 252–260

Abstract: Peroxisome targeting signal (PTS)2 directs proteins from their site of synthesis in the cytosol to the lumen of the peroxisome. Unlike PTS1 which is present in the great majority of peroxisomal matrix proteins and whose import mechanics have been ... ...

Abstract	Peroxisome targeting signal (PTS)2 directs proteins from their site of synthesis in the cytosol to the lumen of the peroxisome. Unlike PTS1 which is present in the great majority of peroxisomal matrix proteins and whose import mechanics have been dissected in considerable detail, PTS2 is a relatively rare topogenic signal whose import mechanisms are far less well understood. However, as is the case for PTS1 proteins, an inability to import PTS2 proteins leads to human disease. In this report, we describe the biochemical characterization of mammalian PTS2 protein import using a semi-permeabilized cell system. We show that a PTS2-containing reporter molecule is taken up by peroxisomes in a reaction that is time-, temperature-, ATP-, and cytosol-dependent. Furthermore, the import process is specific, saturable, and requires action of the chaperone Hsc70, the cochaperone Hsp40, and the peroxins Pex5p and Pex14p. We also demonstrate peroxisomal translocation of PTS2 reporter/antibody complexes confirming the import competence of higher order structures. Importantly, cultured fibroblasts from patients with the rhizomelic form of chondrodysplasia punctata (RCDP) which are deficient for the PTS2 receptor protein, Pex7p, are unable to import the PTS2 reporter in this assay. The ability to monitor PTS2 import in vitro will permit, for the first time, a detailed comparison of the biochemical properties of PTS1 and PTS2 protein import.
MeSH term(s)	Acetyl-CoA C-Acetyltransferase/genetics ; Acetyl-CoA C-Acetyltransferase/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; CHO Cells ; Cells, Cultured ; Chondrodysplasia Punctata, Rhizomelic/genetics ; Chondrodysplasia Punctata, Rhizomelic/metabolism ; Chondrodysplasia Punctata, Rhizomelic/pathology ; Cricetinae ; Cytosol/metabolism ; Fibroblasts ; Fluorescent Antibody Technique ; HSC70 Heat-Shock Proteins ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/metabolism ; Peroxisomal Targeting Signal 2 Receptor ; Peroxisomes/metabolism ; Protein Transport ; Receptors, Cytoplasmic and Nuclear/deficiency ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Temperature ; Time Factors
Chemical Substances	DNAJB1 protein, human ; HSC70 Heat-Shock Proteins ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; HSPA8 protein, human ; Heat-Shock Proteins ; Molecular Chaperones ; Peroxisomal Targeting Signal 2 Receptor ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; Acetyl-CoA C-Acetyltransferase (EC 2.3.1.9)
Language	English
Publishing date	2001-03-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1034/j.1600-0854.2001.90165.x
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Article ; Online: Reactive oxygen species in tumor necrosis factor-alpha-activated primary human keratinocytes: implications for psoriasis and inflammatory skin disease.

Young, Chen N / Koepke, Jay I / Terlecky, Laura J / Borkin, Michael S / Boyd, Savoy L / Terlecky, Stanley R

The Journal of investigative dermatology

2008 Volume 128, Issue 11, Page(s) 2606–2614

Abstract: The multifunctional cytokine tumor necrosis factor-alpha (TNF-alpha) is known to play an important role in inflammatory and immunological responses in human skin. Although it has been documented that reactive oxygen species (ROS) are involved in TNF- ... ...

Abstract	The multifunctional cytokine tumor necrosis factor-alpha (TNF-alpha) is known to play an important role in inflammatory and immunological responses in human skin. Although it has been documented that reactive oxygen species (ROS) are involved in TNF-alpha-induced signaling pathways associated with certain inflammatory diseases, their role in TNF-alpha signaling cascades has not been examined in primary human keratinocytes used as a model of inflammatory skin disease and psoriasis. Employing a series of in vitro and in cellulo approaches, we have demonstrated that in primary human keratinocytes (i) TNF-alpha rapidly induces ROS generation, IkappaB degradation, NF-kappaB p65 nuclear translocation, and ultimately production of inflammatory cytokines; (ii) TNF-alpha-induced cytokine production is mediated both by the mammalian target of rapamycin signaling pathway via NF-kappaB activation and by ROS; (iii) TNF-alpha-dependent NF-kappaB activation (that is, IkappaB degradation and NF-kappaB p65 nuclear translocation) is not mediated by ROS; and (iv) a cell-penetrating derivative of the antioxidant enzyme, catalase, as well as taurine and N-acetyl-cysteine attenuate the TNF-alpha-induced production of cytokines. These latter results suggest that catalase and perhaps other antioxidants should be considered as part of a more specific and effective therapy for the treatment of inflammatory skin diseases, including psoriasis.
MeSH term(s)	Acetylcysteine/pharmacology ; Antioxidants/therapeutic use ; Catalase/therapeutic use ; Cells, Cultured ; Free Radical Scavengers/pharmacology ; Humans ; Hydrogen Peroxide/metabolism ; Hydrogen Peroxide/pharmacology ; I-kappa B Proteins/metabolism ; Interleukin-6/metabolism ; Interleukin-8/metabolism ; Keratinocytes/cytology ; Keratinocytes/drug effects ; Keratinocytes/metabolism ; Male ; Protein Kinases/metabolism ; Psoriasis/drug therapy ; Psoriasis/metabolism ; Psoriasis/physiopathology ; Reactive Oxygen Species/metabolism ; Signal Transduction/drug effects ; Signal Transduction/physiology ; Sirolimus/pharmacology ; Skin Diseases/drug therapy ; Skin Diseases/metabolism ; Skin Diseases/physiopathology ; TOR Serine-Threonine Kinases ; Taurine/pharmacology ; Transcription Factor RelA/metabolism ; Tumor Necrosis Factor-alpha/metabolism ; Tumor Necrosis Factor-alpha/pharmacology
Chemical Substances	Antioxidants ; Free Radical Scavengers ; I-kappa B Proteins ; Interleukin-6 ; Interleukin-8 ; Reactive Oxygen Species ; Transcription Factor RelA ; Tumor Necrosis Factor-alpha ; Taurine (1EQV5MLY3D) ; Hydrogen Peroxide (BBX060AN9V) ; Catalase (EC 1.11.1.6) ; Protein Kinases (EC 2.7.-) ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Sirolimus (W36ZG6FT64) ; Acetylcysteine (WYQ7N0BPYC)
Language	English
Publishing date	2008-05-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1038/jid.2008.122
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Article: Restoration of peroxisomal catalase import in a model of human cellular aging.

Koepke, Jay I / Nakrieko, Kerry-Ann / Wood, Christopher S / Boucher, Krissy K / Terlecky, Laura J / Walton, Paul A / Terlecky, Stanley R

Traffic (Copenhagen, Denmark)

2007 Volume 8, Issue 11, Page(s) 1590–1600

Abstract: Peroxisomes play an important role in human cellular metabolism by housing enzymes involved in a number of essential biochemical pathways. Many of these enzymes are oxidases that transfer hydrogen atoms to molecular oxygen forming hydrogen peroxide. The ... ...

Abstract	Peroxisomes play an important role in human cellular metabolism by housing enzymes involved in a number of essential biochemical pathways. Many of these enzymes are oxidases that transfer hydrogen atoms to molecular oxygen forming hydrogen peroxide. The organelle also contains catalase, which readily decomposes the hydrogen peroxide, a potentially damaging oxidant. Previous work has demonstrated that aging compromises peroxisomal protein import with catalase being particularly affected. The resultant imbalance in the relative ratio of oxidases to catalase was seen as a potential contributor to cellular oxidative stress and aging. Here we report that altering the peroxisomal targeting signal of catalase to the more effective serine-lysine-leucine (SKL) sequence results in a catalase molecule that more strongly interacts with its receptor and is more efficiently imported in both in vitro and in vivo assays. Furthermore, catalase-SKL monomers expressed in cells interact with endogenous catalase subunits resulting in altered trafficking of the latter molecules. A dramatic reduction in cellular hydrogen peroxide levels accompanies this increased peroxisomal import of catalase. Finally, we show that catalase-SKL stably expressed in cells by retroviral-mediated transduction repolarizes mitochondria and reduces the number of senescent cells in a population. These results demonstrate the utility of a catalase-SKL therapy for the restoration of a normal oxidative state in aging cells.
MeSH term(s)	Animals ; Biochemistry/methods ; CHO Cells ; Catalase/chemistry ; Catalase/metabolism ; Cell Line, Tumor ; Cellular Senescence ; Cricetinae ; Cricetulus ; Fibroblasts/metabolism ; Humans ; Oxidoreductases/chemistry ; Peroxisomes/enzymology ; Peroxisomes/metabolism ; Reactive Oxygen Species ; Signal Transduction ; Surface Plasmon Resonance ; Time Factors
Chemical Substances	Reactive Oxygen Species ; Oxidoreductases (EC 1.-) ; Catalase (EC 1.11.1.6)
Language	English
Publishing date	2007-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/j.1600-0854.2007.00633.x
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